ID   VHR1_VIOHE              Reviewed;          30 AA.
AC   P83937;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Root cyclotide 1;
DE   AltName: Full=Vhr1;
OS   Viola hederacea (Australian violet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Violaceae; Viola.
OX   NCBI_TaxID=180952;
RN   [1]
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, MASS SPECTROMETRY, STRUCTURE BY NMR,
RP   AND DISULFIDE BONDS.
RC   TISSUE=Root;
RX   PubMed=15295104; DOI=10.1105/tpc.104.021790;
RA   Trabi M., Craik D.J.;
RT   "Tissue-specific expression of head-to-tail cyclized miniproteins in
RT   Violaceae and structure determination of the root cyclotide Viola hederacea
RT   root cyclotide1.";
RL   Plant Cell 16:2204-2216(2004).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism.
CC   -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:15295104}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- PTM: This is a cyclic peptide.
CC   -!- MASS SPECTROMETRY: Mass=3115; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15295104};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- CAUTION: This peptide is cyclic. The start position was chosen by
CC       similarity to OAK1 (kalata-B1) for which the DNA sequence is known.
CC       {ECO:0000305}.
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DR   PDB; 1VB8; NMR; -; A=4-30.
DR   PDBsum; 1VB8; -.
DR   AlphaFoldDB; P83937; -.
DR   SMR; P83937; -.
DR   EvolutionaryTrace; P83937; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012323; Cyclotide_bracelet_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   PIRSF; PIRSF037891; Cycloviolacin; 1.
DR   SUPFAM; SSF57038; SSF57038; 1.
DR   PROSITE; PS51052; CYCLOTIDE; 1.
DR   PROSITE; PS60008; CYCLOTIDE_BRACELET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Knottin;
KW   Plant defense.
FT   PEPTIDE         1..30
FT                   /note="Root cyclotide 1"
FT                   /id="PRO_0000043608"
FT   DISULFID        4..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:15295104"
FT   DISULFID        8..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:15295104"
FT   DISULFID        13..28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:15295104"
FT   CROSSLNK        1..30
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:1VB8"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:1VB8"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:1VB8"
FT   STRAND          23..28
FT                   /evidence="ECO:0007829|PDB:1VB8"
SQ   SEQUENCE   30 AA;  3136 MW;  B6F6DAD5686B2937 CRC64;
     GIPCAESCVW IPCTVTALLG CSCSNKVCYN